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Contents |
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208 a.a.
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14 a.a.
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11 a.a.
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12 a.a.
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* Residue conservation analysis
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PDB id:
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| Name: |
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Antitumor protein
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Title:
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Structural basis of phospho-peptide recognition by the brct domain of brca1, structure with phosphopeptide
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Structure:
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Breast cancer type 1 susceptibility protein. Chain: a, b, c, d, e. Fragment: brct domain 1646-1859. Engineered: yes. Brctide-7ps. Chain: f, g, h, i, j. Engineered: yes. Other_details: in vitro optimized phosphopeptide
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: brca1. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: in vitro optimized phosphopeptide
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Biol. unit:
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Dimer (from
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Resolution:
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3.30Å
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R-factor:
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0.261
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R-free:
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0.301
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Authors:
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R.S.Williams,M.S.Lee,D.D.Hau,J.N.M.Glover
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Key ref:
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R.S.Williams
et al.
(2004).
Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1.
Nat Struct Mol Biol,
11,
519-525.
PubMed id:
DOI:
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Date:
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22-Apr-04
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Release date:
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11-May-04
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PROCHECK
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Headers
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References
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P38398
(BRCA1_HUMAN) -
Breast cancer type 1 susceptibility protein from Homo sapiens
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Seq:
Struc:
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1863 a.a.
208 a.a.
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No UniProt id for this chain
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Enzyme class:
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Chains A, B, C, D, E:
E.C.2.3.2.27
- RING-type E3 ubiquitin transferase.
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Reaction:
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6- ubiquitinyl-[acceptor protein]-L-lysine
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DOI no:
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Nat Struct Mol Biol
11:519-525
(2004)
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PubMed id:
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Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1.
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R.S.Williams,
M.S.Lee,
D.D.Hau,
J.N.Glover.
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ABSTRACT
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The BRCT repeats in BRCA1 are essential for its tumor suppressor activity and
interact with phosphorylated protein targets containing the sequence
pSer-X-X-Phe, where X indicates any residue. The structure of the tandem BRCA1
BRCT repeats bound to an optimized phosphopeptide reveals that the N-terminal
repeat harbors a conserved BRCT phosphoserine-binding pocket, while the
interface between the repeats forms a hydrophobic groove that recognizes the
phenylalanine. Crystallographic and biochemical data suggest that the structural
integrity of both binding sites is essential for peptide recognition. The
diminished peptide-binding capacity observed for cancer-associated BRCA1-BRCT
variants may explain the enhanced cancer risks associated with these mutations.
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Selected figure(s)
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Figure 1.
Figure 1. Overview of the BRCA1 BRCT -peptide complex. (a)
 -strands
in the BRCT domain are green and  -helices
are yellow. The peptide is blue. The BRCT residues that
recognize the pSer and Phe(+3) residues have transparent
surfaces. (b) Amino acid sequence of the human BRCA1 BRCT domain
with secondary structure. The residues that contact the
phosphoserine are shaded blue, and those that form the
Phe(+3)-binding pocket are marked by red circles. Missense
mutations assayed for interactions with the peptide are above
the sequence. Residues involved in inter-repeat BRCT
interactions are boxed. (c) Structural arrangement of one of the
three similar dimers in the crystallographic asymmetric unit.
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Figure 2.
Figure 2. Details of BRCA1 BRCT -peptide interactions. (a)
Stereo view of key residues that recognize the pSer and Phe(+3)
residues of the peptide. Hydrogen bonds and salt bridges are
indicated by dotted lines. (b) Conformational variability of
phosphopeptide binding. Overlay of the five independent peptide
structures in the crystallographic asymmetric unit. The BRCT C
atoms
of each of the BRCT -peptide complexes were superimposed to
generate the overlay. (c) Electrostatic surface representation
of the BRCT domain with the pSer- and Phe-binding pockets; the
peptide is gray.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Mol Biol
(2004,
11,
519-525)
copyright 2004.
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Figures were
selected
by the author.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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C.C.Leung,
E.Kellogg,
A.Kuhnert,
F.Hänel,
D.Baker,
and
J.N.Glover
(2010).
Insights from the crystal structure of the sixth BRCT domain of topoisomerase IIbeta binding protein 1.
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Protein Sci,
19,
162-167.
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PDB code:
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J.S.Williams,
R.S.Williams,
C.L.Dovey,
G.Guenther,
J.A.Tainer,
and
P.Russell
(2010).
gammaH2A binds Brc1 to maintain genome integrity during S-phase.
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EMBO J,
29,
1136-1148.
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PDB codes:
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M.E.Moynahan,
and
M.Jasin
(2010).
Mitotic homologous recombination maintains genomic stability and suppresses tumorigenesis.
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Nat Rev Mol Cell Biol,
11,
196-207.
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|
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M.W.Richards,
J.W.Leung,
S.M.Roe,
K.Li,
J.Chen,
and
R.Bayliss
(2010).
A pocket on the surface of the N-terminal BRCT domain of Mcph1 is required to prevent abnormal chromosome condensation.
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J Mol Biol,
395,
908-915.
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PDB code:
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P.R.Joseph,
Z.Yuan,
E.A.Kumar,
G.L.Lokesh,
S.Kizhake,
K.Rajarathnam,
and
A.Natarajan
(2010).
Structural characterization of BRCT-tetrapeptide binding interactions.
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Biochem Biophys Res Commun,
393,
207-210.
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S.J.Campbell,
R.A.Edwards,
and
J.N.Glover
(2010).
Comparison of the structures and peptide binding specificities of the BRCT domains of MDC1 and BRCA1.
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Structure,
18,
167-176.
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PDB codes:
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S.Rajasekaran,
T.Mi,
J.C.Merlin,
A.Oommen,
P.Gradie,
and
M.R.Schiller
(2010).
Partitioning of minimotifs based on function with improved prediction accuracy.
|
| |
PLoS One,
5,
e12276.
|
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|
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|
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A.De Nicolo,
E.Parisini,
Q.Zhong,
M.Dalla Palma,
K.A.Stoeckert,
S.M.Domchek,
K.L.Nathanson,
M.A.Caligo,
M.Vidal,
M.E.Cusick,
and
J.E.Garber
(2009).
Multimodal assessment of protein functional deficiency supports pathogenicity of BRCA1 p.V1688del.
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Cancer Res,
69,
7030-7037.
|
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|
|
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|
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I.Drikos,
G.Nounesis,
and
C.E.Vorgias
(2009).
Characterization of cancer-linked BRCA1-BRCT missense variants and their interaction with phosphoprotein targets.
|
| |
Proteins,
77,
464-476.
|
|
|
|
|
|
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M.Carvalho,
M.A.Pino,
R.Karchin,
J.Beddor,
M.Godinho-Netto,
R.D.Mesquita,
R.S.Rodarte,
D.C.Vaz,
V.A.Monteiro,
S.Manoukian,
M.Colombo,
C.B.Ripamonti,
R.Rosenquist,
G.Suthers,
A.Borg,
P.Radice,
S.A.Grist,
A.N.Monteiro,
and
B.Billack
(2009).
Analysis of a set of missense, frameshift, and in-frame deletion variants of BRCA1.
|
| |
Mutat Res,
660,
1.
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|
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R.S.Williams,
G.E.Dodson,
O.Limbo,
Y.Yamada,
J.S.Williams,
G.Guenther,
S.Classen,
J.N.Glover,
H.Iwasaki,
P.Russell,
and
J.A.Tainer
(2009).
Nbs1 flexibly tethers Ctp1 and Mre11-Rad50 to coordinate DNA double-strand break processing and repair.
|
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Cell,
139,
87-99.
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PDB codes:
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T.Usui,
S.S.Foster,
and
J.H.Petrini
(2009).
Maintenance of the DNA-damage checkpoint requires DNA-damage-induced mediator protein oligomerization.
|
| |
Mol Cell,
33,
147-159.
|
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|
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|
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A.De Nicolo,
M.Tancredi,
G.Lombardi,
C.C.Flemma,
S.Barbuti,
C.Di Cristofano,
B.Sobhian,
G.Bevilacqua,
R.Drapkin,
and
M.A.Caligo
(2008).
A novel breast cancer-associated BRIP1 (FANCJ/BACH1) germ-line mutation impairs protein stability and function.
|
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Clin Cancer Res,
14,
4672-4680.
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|
|
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|
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A.Ghosh,
S.Shuman,
and
C.D.Lima
(2008).
The structure of Fcp1, an essential RNA polymerase II CTD phosphatase.
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Mol Cell,
32,
478-490.
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PDB codes:
|
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A.Kinner,
W.Wu,
C.Staudt,
and
G.Iliakis
(2008).
Gamma-H2AX in recognition and signaling of DNA double-strand breaks in the context of chromatin.
|
| |
Nucleic Acids Res,
36,
5678-5694.
|
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A.Kumar,
W.S.Joo,
G.Meinke,
S.Moine,
E.N.Naumova,
and
P.A.Bullock
(2008).
Evidence for a structural relationship between BRCT domains and the helicase domains of the replication initiators encoded by the Polyomaviridae and Papillomaviridae families of DNA tumor viruses.
|
| |
J Virol,
82,
8849-8862.
|
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C.Xu,
L.Wu,
G.Cui,
M.V.Botuyan,
J.Chen,
and
G.Mer
(2008).
Structure of a second BRCT domain identified in the nijmegen breakage syndrome protein Nbs1 and its function in an MDC1-dependent localization of Nbs1 to DNA damage sites.
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J Mol Biol,
381,
361-372.
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PDB code:
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F.J.Couch,
L.J.Rasmussen,
R.Hofstra,
A.N.Monteiro,
M.S.Greenblatt,
N.de Wind,
P.Boffetta,
F.Couch,
N.de Wind,
D.Easton,
D.Eccles,
W.Foulkes,
M.Genuardi,
D.Goldgar,
M.Greenblatt,
R.Hofstra,
F.Hogervorst,
N.Hoogerbrugge,
S.Plon,
P.Radice,
L.Rasmussen,
O.Sinilnikova,
A.Spurdle,
and
S.V.Tavtigian
(2008).
Assessment of functional effects of unclassified genetic variants.
|
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Hum Mutat,
29,
1314-1326.
|
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|
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|
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J.Brunet,
A.Vazquez-Martin,
R.Colomer,
B.Graña-Suarez,
B.Martin-Castillo,
and
J.A.Menendez
(2008).
BRCA1 and acetyl-CoA carboxylase: the metabolic syndrome of breast cancer.
|
| |
Mol Carcinog,
47,
157-163.
|
|
|
|
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|
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M.Tischkowitz,
N.Hamel,
M.A.Carvalho,
G.Birrane,
A.Soni,
E.H.van Beers,
S.A.Joosse,
N.Wong,
D.Novak,
L.A.Quenneville,
S.A.Grist,
P.M.Nederlof,
D.E.Goldgar,
S.V.Tavtigian,
A.N.Monteiro,
J.A.Ladias,
and
W.D.Foulkes
(2008).
Pathogenicity of the BRCA1 missense variant M1775K is determined by the disruption of the BRCT phosphopeptide-binding pocket: a multi-modal approach.
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Eur J Hum Genet,
16,
820-832.
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PDB code:
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R.A.Edwards,
M.S.Lee,
S.E.Tsutakawa,
R.S.Williams,
J.A.Tainer,
and
J.N.Glover
(2008).
The BARD1 C-terminal domain structure and interactions with polyadenylation factor CstF-50.
|
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Biochemistry,
47,
11446-11456.
|
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R.S.Williams,
G.Moncalian,
J.S.Williams,
Y.Yamada,
O.Limbo,
D.S.Shin,
L.M.Groocock,
D.Cahill,
C.Hitomi,
G.Guenther,
D.Moiani,
J.P.Carney,
P.Russell,
and
J.A.Tainer
(2008).
Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair.
|
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Cell,
135,
97.
|
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PDB codes:
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T.Anagnostopoulos,
M.Pertesi,
I.Konstantopoulou,
S.Armaou,
S.Kamakari,
G.Nasioulas,
A.Athanasiou,
A.Dobrovic,
M.A.Young,
D.Goldgar,
G.Fountzilas,
and
D.Yannoukakos
(2008).
G1738R is a BRCA1 founder mutation in Greek breast/ovarian cancer patients: evaluation of its pathogenicity and inferences on its genealogical history.
|
| |
Breast Cancer Res Treat,
110,
377-385.
|
|
|
|
|
|
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Y.Nominé,
M.V.Botuyan,
Z.Bajzer,
W.G.Owen,
A.J.Caride,
E.Wasielewski,
and
G.Mer
(2008).
Kinetic analysis of interaction of BRCA1 tandem breast cancer c-terminal domains with phosphorylated peptides reveals two binding conformations.
|
| |
Biochemistry,
47,
9866-9879.
|
|
|
|
|
|
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Y.Shen,
and
L.Tong
(2008).
Structural evidence for direct interactions between the BRCT domains of human BRCA1 and a phospho-peptide from human ACC1.
|
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Biochemistry,
47,
5767-5773.
|
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PDB code:
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C.A.Gough,
T.Gojobori,
and
T.Imanishi
(2007).
Cancer-related mutations in BRCA1-BRCT cause long-range structural changes in protein-protein binding sites: a molecular dynamics study.
|
| |
Proteins,
66,
69-86.
|
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|
|
|
|
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E.F.DeRose,
M.W.Clarkson,
S.A.Gilmore,
C.J.Galban,
A.Tripathy,
J.M.Havener,
G.A.Mueller,
D.A.Ramsden,
R.E.London,
and
A.L.Lee
(2007).
Solution structure of polymerase mu's BRCT Domain reveals an element essential for its role in nonhomologous end joining.
|
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Biochemistry,
46,
12100-12110.
|
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PDB code:
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M.A.Carvalho,
S.M.Marsillac,
R.Karchin,
S.Manoukian,
S.Grist,
R.F.Swaby,
T.P.Urmenyi,
E.Rondinelli,
R.Silva,
L.Gayol,
L.Baumbach,
R.Sutphen,
J.L.Pickard-Brzosowicz,
K.L.Nathanson,
A.Sali,
D.Goldgar,
F.J.Couch,
P.Radice,
and
A.N.Monteiro
(2007).
Determination of cancer risk associated with germ line BRCA1 missense variants by functional analysis.
|
| |
Cancer Res,
67,
1494-1501.
|
|
|
|
|
|
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M.Hölzel,
T.Grimm,
M.Rohrmoser,
A.Malamoussi,
T.Harasim,
A.Gruber-Eber,
E.Kremmer,
and
D.Eick
(2007).
The BRCT domain of mammalian Pes1 is crucial for nucleolar localization and rRNA processing.
|
| |
Nucleic Acids Res,
35,
789-800.
|
|
|
|
|
|
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M.Laufer,
S.V.Nandula,
A.P.Modi,
S.Wang,
M.Jasin,
V.V.Murty,
T.Ludwig,
and
R.Baer
(2007).
Structural requirements for the BARD1 tumor suppressor in chromosomal stability and homology-directed DNA repair.
|
| |
J Biol Chem,
282,
34325-34333.
|
|
|
|
|
|
|
P.Vasickova,
E.Machackova,
M.Lukesova,
J.Damborsky,
O.Horky,
H.Pavlu,
J.Kuklova,
V.Kosinova,
M.Navratilova,
and
L.Foretova
(2007).
High occurrence of BRCA1 intragenic rearrangements in hereditary breast and ovarian cancer syndrome in the Czech Republic.
|
| |
BMC Med Genet,
8,
32.
|
|
|
|
|
|
|
R.Karchin,
A.N.Monteiro,
S.V.Tavtigian,
M.A.Carvalho,
and
A.Sali
(2007).
Functional impact of missense variants in BRCA1 predicted by supervised learning.
|
| |
PLoS Comput Biol,
3,
e26.
|
|
|
|
|
|
|
R.S.Williams,
J.S.Williams,
and
J.A.Tainer
(2007).
Mre11-Rad50-Nbs1 is a keystone complex connecting DNA repair machinery, double-strand break signaling, and the chromatin template.
|
| |
Biochem Cell Biol,
85,
509-520.
|
|
|
|
|
|
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Z.Liu,
J.Wu,
and
X.Yu
(2007).
CCDC98 targets BRCA1 to DNA damage sites.
|
| |
Nat Struct Mol Biol,
14,
716-720.
|
|
|
|
|
|
|
D.C.Zappulla,
A.S.Maharaj,
J.J.Connelly,
R.A.Jockusch,
and
R.Sternglanz
(2006).
Rtt107/Esc4 binds silent chromatin and DNA repair proteins using different BRCT motifs.
|
| |
BMC Mol Biol,
7,
40.
|
|
|
|
|
|
|
J.Liu,
Y.Pan,
B.Ma,
and
R.Nussinov
(2006).
"Similarity trap" in protein-protein interactions could be carcinogenic: simulations of p53 core domain complexed with 53BP1 and BRCA1 BRCT domains.
|
| |
Structure,
14,
1811-1821.
|
|
|
|
|
|
|
J.N.Glover
(2006).
Insights into the molecular basis of human hereditary breast cancer from studies of the BRCA1 BRCT domain.
|
| |
Fam Cancer,
5,
89-93.
|
|
|
|
|
|
|
M.Kobayashi,
F.Figaroa,
N.Meeuwenoord,
L.E.Jansen,
and
G.Siegal
(2006).
Characterization of the DNA binding and structural properties of the BRCT region of human replication factor C p140 subunit.
|
| |
J Biol Chem,
281,
4308-4317.
|
|
|
|
|
|
|
P.K.Lovelock,
S.Healey,
W.Au,
E.Y.Sum,
A.Tesoriero,
E.M.Wong,
S.Hinson,
R.Brinkworth,
A.Bekessy,
O.Diez,
L.Izatt,
E.Solomon,
M.Jenkins,
H.Renard,
J.Hopper,
P.Waring,
S.V.Tavtigian,
D.Goldgar,
G.J.Lindeman,
J.E.Visvader,
F.J.Couch,
B.R.Henderson,
M.Southey,
G.Chenevix-Trench,
A.B.Spurdle,
and
M.A.Brown
(2006).
Genetic, functional, and histopathological evaluation of two C-terminal BRCA1 missense variants.
|
| |
J Med Genet,
43,
74-83.
|
|
|
|
|
|
|
S.Agata,
A.Viel,
L.Della Puppa,
L.Cortesi,
G.Fersini,
M.Callegaro,
M.Dalla Palma,
R.Dolcetti,
M.Federico,
S.Venuta,
G.Miolo,
E.D'Andrea,
and
M.Montagna
(2006).
Prevalence of BRCA1 genomic rearrangements in a large cohort of Italian breast and breast/ovarian cancer families without detectable BRCA1 and BRCA2 point mutations.
|
| |
Genes Chromosomes Cancer,
45,
791-797.
|
|
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B.A.Joughin,
B.Tidor,
and
M.B.Yaffe
(2005).
A computational method for the analysis and prediction of protein:phosphopeptide-binding sites.
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Protein Sci,
14,
131-139.
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M.S.Lee,
R.A.Edwards,
G.L.Thede,
and
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(2005).
Structure of the BRCT repeat domain of MDC1 and its specificity for the free COOH-terminal end of the gamma-H2AX histone tail.
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| |
J Biol Chem,
280,
32053-32056.
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PDB code:
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M.Stucki,
J.A.Clapperton,
D.Mohammad,
M.B.Yaffe,
S.J.Smerdon,
and
S.P.Jackson
(2005).
MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks.
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| |
Cell,
123,
1213-1226.
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PDB code:
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R.S.Williams,
N.Bernstein,
M.S.Lee,
M.L.Rakovszky,
D.Cui,
R.Green,
M.Weinfeld,
and
J.N.Glover
(2005).
Structural basis for phosphorylation-dependent signaling in the DNA-damage response.
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Biochem Cell Biol,
83,
721-727.
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W.L.Bridge,
C.J.Vandenberg,
R.J.Franklin,
and
K.Hiom
(2005).
The BRIP1 helicase functions independently of BRCA1 in the Fanconi anemia pathway for DNA crosslink repair.
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Nat Genet,
37,
953-957.
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G.Charier,
J.Couprie,
B.Alpha-Bazin,
V.Meyer,
E.Quéméneur,
R.Guérois,
I.Callebaut,
B.Gilquin,
and
S.Zinn-Justin
(2004).
The Tudor tandem of 53BP1: a new structural motif involved in DNA and RG-rich peptide binding.
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| |
Structure,
12,
1551-1562.
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PDB code:
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J.A.Clapperton,
I.A.Manke,
D.M.Lowery,
T.Ho,
L.F.Haire,
M.B.Yaffe,
and
S.J.Smerdon
(2004).
Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer.
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| |
Nat Struct Mol Biol,
11,
512-518.
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PDB code:
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J.N.Glover,
R.S.Williams,
and
M.S.Lee
(2004).
Interactions between BRCT repeats and phosphoproteins: tangled up in two.
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Trends Biochem Sci,
29,
579-585.
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X.Yu,
and
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(2004).
DNA damage-induced cell cycle checkpoint control requires CtIP, a phosphorylation-dependent binding partner of BRCA1 C-terminal domains.
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Mol Cell Biol,
24,
9478-9486.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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